Lignin is a major component of all plants, the degradation of which remains a major challenge to date owing to its recalcitrant nature. Several classes of fungi have been studied to carry out this process to some extent, but overall the process remains inefficient. We have isolated a novel alkalophilic dimorphic lignin-degrading Deuteromycete from soil, identified as “uncultured” and coded as MVI.2011. Supernatant from 12-h culture of MVI.2011 in optimized mineral medium containing lignin pH 9.0 was analysed for Lignin Peroxidase, Manganese Peroxidase and Laccase. Enzyme purification was carried out by standard protocols using ammonium sulphate precipitation followed by further purification by Gel Permeation Chromatography. Analysis of total protein, specific enzyme activity and molecular weight of the GPC-purified LiP, MnP and Laccase showed 93.83 μg/ml, 5.27 U/mg, 42 kDa; 78.13 μg/ml, 13.18 U/mg, 45 kDa and 85.81 μg/ml, 4.77 U/mg, 62 kDa, respectively. The purified enzymes possessed high activity over a wide range of pH (4–11), and temperature (30–55 °C). The optimum substrate concentration was 20 μg/ml of lignin for all the three enzymes. CD spectra suggested that the predominant secondary structure was helix in LiP, and, turns in MnP and Laccase. The breakdown products of lignin degradation by MVI.2011 and the three purified enzymes were detected and identified by FTIR and GC–MS. They were oxalic acid, hentriacontane, derivatives of octadecane, nonane, etc. These vital compounds are certain to find application as biofuels, an alternate energy source in various industries.Electronic supplementary materialThe online version of this article (doi:10.1007/s13205-016-0384-z) contains supplementary material, which is available to authorized users.

Plants belonging to Rubiaceae family have been used in Chinese folk medicine and Ayurveda. The aim of the study was to determine the effect of Mussaenin A isolated from root of Mussaenda glabrata on liver cancer cell line, Hep G2. MTT assay was performed to check the ability of Mussaenin A to induce death in cancerous Hep G2 cells and normal NIH3T3 cells. Acridine Orange/Ethidium Bromide staining, Hoechst staining and DNA fragmentation assays were used to confirm the apoptosis inducing ability of MA on Hep G2 cells. RT-PCR and western blotting was performed to check the expression of pro- and anti-apoptotic factors. Calorimetric assay was done to check caspase-3 and caspase-9 activities. Mussaenin A at lower concentrations was found to induce cell death selectively in the liver cancer cells (IC50 = 11.38 µg/mL). The transcriptional expression studies of the pro-apoptotic Bax and anti-apoptotic Bcl-2 and Cox-2; and the western blot analysis of pro-apoptotic BAK and BAD showed that MA upregulated the expression of pro-apoptotic factors and down regulated the expression of anti-apoptotic factors in Hep G2 cells. Caspase-9 and 3 activities were found to be upregulated in the calorimetric studies. The down regulation of anti-apoptotic factors and upregulation of pro-apoptotic factors show that the Mussaenin A induced apoptosis in the liver cancer cells via the intrinsic or the mitochondrial pathway.